Homo sapiens · seed Q71U36 · 451 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt Q71U36 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 3.40.50.1440 CATH 3.30.1330.20 CATH 1.10.287.600 SCOP 8044258 SCOP 8034386 SCOP 8034383 SCOP 8044257 SCOP 8034387 SCOP 8036011 SCOP 8034385 SCOP 8036009 RCSB 9WD9 PDBe
CATH and SCOP identifiers come from the RCSB's own structure annotations, which the Domains panel already reads, so these are looked up rather than guessed at.
Every figure here is counted over the whole family rather than quoted from one entry.
9WD9, the structure every other member of this family is superposed onto. Rendered by the RCSB and embedded here: the live app shows an interactive viewport, which a document that fetches nothing cannot.
How many of this family's constructs contain each residue of the seed. A trough is a stretch nobody has put in a construct, which is a construct-design answer rather than a disorder one.
169 distinct constructs across 866 entries. 476 polymer entities differ from the UniProt canonical sequence in some way, 25 carry a recognised expression tag and 0 carry a fusion partner.
"Differs from canonical" is not the same as "engineered". The canonical sequence is the full gene product, so a secreted protein whose structures all start after its signal peptide counts every one of them as different: lysozyme's most-used construct, residues 19–147 on 1,239 entities, is simply the mature protein. Read the construct column below for what was actually done, rather than this count.
| Entities | Length | Best (Å) | Best entry | What was made |
|---|---|---|---|---|
| 394 | 451 | 1.70 | 8QL2 | matches the canonical sequence |
| 337 | 445 | 1.52 | 6S8K | matches the canonical sequence |
| 109 | 445 | 2.21 | 7L05 | matches the canonical sequence |
| 66 | 450 | 1.80 | 4I4T | residues 1-450 |
| 46 | 440 | 2.25 | 6S9E | residues 1-440 |
| 40 | 431 | 2.37 | 8YUA | residues 1-431 |
| 33 | 451 | 2.26 | 9WD9 | matches the canonical sequence |
| 33 | 451 | 3.50 | 1JFF | L136S, S232G, I265G +2 more |
| 27 | 444 | 2.21 | 9M1M | matches the canonical sequence |
| 22 | 445 | 2.80 | 8SH7 | matches the canonical sequence |
| 21 | 451 | 2.88 | 7X4N | matches the canonical sequence |
| 19 | 445 | 3.60 | 7ZCW | T55A, M170V, S296A +1 more |
| 18 | 451 | 3.57 | 8RX1 | matches the canonical sequence |
| 13 | 445 | 2.50 | 5KX5 | matches the canonical sequence |
| 12 | 426 | 3.62 | 6KIQ | residues 2-427 |
| 12 | 427 | 2.80 | 9DUQ | residues 1-427 |
| 12 | 438 | 2.10 | 7TTF | residues 1-438 |
| 12 | 452 | 8.20 | 2XRP | V7I, L114I, L136S +5 more |
| 12 | 456 | 2.66 | 8VT7 | TEV site |
| 11 | 426 | 3.20 | 9KBW | residues 1-426 |
| 11 | 443 | 1.75 | 7PJE | matches the canonical sequence |
| 11 | 450 | 1.80 | 6S8L | matches the canonical sequence |
| 10 | 443 | 3.10 | 8GLV | matches the canonical sequence |
| 10 | 449 | 1.75 | 7PJE | matches the canonical sequence |
| 10 | 451 | 3.10 | 8GLV | matches the canonical sequence |
Showing the 25 most-used of 169.
Columns where the wild-type residue still dominates but a real minority carries something else, which is a different question from "what varies across species".
| Oligomeric state | Chains | Entries | Share |
|---|---|---|---|
| hexameric | 6 | 332 | 38.3% |
| trimeric | 3 | 140 | 16.2% |
| pentameric | 5 | 72 | 8.3% |
| tetrameric | 4 | 41 | 4.7% |
| dimeric | 2 | 36 | 4.2% |
| dodecameric | 12 | 33 | 3.8% |
| monomeric | 1 | 17 | 2.0% |
| nonameric | 9 | 15 | 1.7% |
312 entries have the depositor's assembly corroborated by PISA, 529 carry the depositor's word alone and 18 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 1 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 6GVN.
Every source's own domains on the seed axis, one row each. They are not merged: Pfam, CATH, SCOP and InterPro disagree about boundaries, and a merged track would state a consensus none of them gave.
| Domain | Source | Span (seed) | Chains |
|---|---|---|---|
| Tubulin/FtsZ, GTPase domain | CATH 3.40.50.1440 | 1–259 | 598 |
| Tubulin/FtsZ, C-terminal domain | CATH 3.30.1330.20 | 269–376 | 590 |
| Helix hairpin bin | CATH 1.10.287.600 | 377–430 | 482 |
| Tubulin nucleotide-binding domain-like | SCOP2B 8044258 | 1–243 | 125 |
| Tubulin nucleotide-binding domain-like | SCOP2B 8034386 | 2–243 | 275 |
| Tubulin nucleotide-binding domain-like | SCOP2B 8034383 | 2–245 | 261 |
| Tubulin nucleotide-binding domain-like | SCOP2B 8044257 | 2–245 | 30 |
| Tubulin C-terminal domain-like | SCOP2B 8034387 | 244–427 | 275 |
| Tubulin C-terminal domain-like | SCOP2B 8036011 | 244–427 | 125 |
| Tubulin C-terminal domain-like | SCOP2B 8034385 | 246–438 | 261 |
| Tubulin C-terminal domain-like | SCOP2B 8036009 | 246–439 | 30 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| GTP | cofactor | Guanosine-5'-Triphosphate | 772 | 1.25 |
| MG | ion | Magnesium Ion | 730 | 1.52 |
| GDP | cofactor | Guanosine-5'-Diphosphate | 681 | 1.25 |
| CA | ion | Calcium Ion | 325 | 1.70 |
| MES | buffer | 2-(N-Morpholino)-Ethanesulfonic Acid | 289 | 1.80 |
| ACP | cofactor | Phosphomethylphosphonic Acid Adenylate Ester | 273 | 1.80 |
| TA1 | ligand | Taxol | 133 | 2.35 |
| GOL | cryoprotectant | Glycerol | 101 | 1.80 |
| G2P | ligand | Phosphomethylphosphonic Acid Guanylate Ester | 60 | 2.26 |
| ANP | cofactor | Phosphoaminophosphonic Acid-Adenylate Ester | 55 | 2.41 |
| ADP | cofactor | Adenosine-5'-Diphosphate | 52 | 2.00 |
| CL | ion | Chloride Ion | 42 | 1.80 |
| ZN | ion | Zinc Ion | 32 | 2.60 |
| SO4 | ion | Sulfate Ion | 32 | 1.90 |
| IMD | buffer | Imidazole | 31 | 1.90 |
| LOC | ligand | N-[(7s)-1,2,3,10-Tetramethoxy-9-Oxo-6,7-Dihydro-5h-Benzo[D]hepta | 17 | 1.90 |
| AF3 | ligand | Aluminum Fluoride | 17 | 2.21 |
| ATP | cofactor | Adenosine-5'-Triphosphate | 15 | 2.90 |
| NA | ion | Sodium Ion | 10 | 1.25 |
| EDO | cryoprotectant | 1,2-Ethanediol | 10 | 1.90 |
Parsed from the free text 427 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 431
entries that recorded anything at all.
Median pH 6.7
(range 5.5 to 9.0).
838 entries carry a wwPDB validation report: 525 clean, 211 worth a check and 102 with something to explain. Median clashscore 6.57, median RSRZ outliers 3.72%, median R-free minus R-work 0.041. 831 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Bos taurus | 307 | 1.52 | 590 | 100% |
| Sus scrofa | 305 | 1.92 | 568 | 100% |
| Homo sapiens | 88 | 1.80 | 114 | 100% |
| Ovis aries | 38 | 1.90 | 75 | 100% |
| Mus musculus | 25 | 3.19 | 34 | 100% |
| Tetrahymena thermophila | 11 | 1.75 | 22 | 100% |
| Chlamydomonas reinhardtii | 10 | 3.10 | 20 | 100% |
| Drosophila melanogaster | 9 | 2.20 | 18 | 99% |
| Saccharomyces cerevisiae | 9 | 2.81 | 9 | 98% |
| Sus barbatus | 7 | 2.19 | 13 | 100% |
| Saccharomyces cerevisiae S288C | 8 | 2.88 | 12 | 98% |
| Candidatus Odinarchaeum yellowstonii | 11 | 1.25 | 10 | 96% |
451 residues, numbered every ten. Every identity figure in this document is measured against this sequence.
active or binding site modified residue or glycosylation disulphide cysteine transmembrane or signal the 15 most-substituted positions
Sites are UniProt's curated features where the seed is a UniProt accession; the substituted positions are measured from this family's own alignment rather than annotated, and only the fifteen most substituted are marked: every position carrying a minority substitution would be most of the protein, because the family holds orthologues. A residue can carry more than one and is drawn with the first that applies, in the order of the key above.
One record per paper, not per entry.
| Year | Citation |
|---|---|
| 2026 | An evolution-conserved allosteric network in human tubulin governs paclitaxel efficacy. Nat.Chem.Biol. doi:10.1038/s41589-026-02204-2 |
| 2026 | Structure and dynamics of a four-protofilament microtubule from Heimdallarchaeales alpha / beta-tubulin. Sci Adv doi:10.1126/sciadv.aeh4305 |
| 2026 | Bacteria deliver a microtubule-binding protein into mammalian cells to promote colonization. Science doi:10.1126/science.adz2737 |
| 2026 | Structure-based design and synthesis of KX-01 analogs as potent antitumor agents targeting the tubulin colchicine binding site. Eur.J.Med.Chem. doi:10.1016/j.ejmech.2026.118849 |
| 2026 | Cryo-EM structure of the human Hec1-Nuf2 dimer bound to the paclitaxel-stabilized microtubule Sci Adv |
| 2026 | Microtubules in the axon are GDP bound but adopt a stable GTP-like expanded state. Nat.Struct.Mol.Biol. doi:10.1038/s41594-026-01787-7 |
| 2026 | A cryo-EM processing pipeline for microtubules using CryoSPARC. Acta Crystallogr D Struct Biol doi:10.1107/S2059798326003062 |
| 2026 | Molecular insight into microtubule nucleation by the XMAP215/ gamma-TuRC module. Nat Commun doi:10.1038/s41467-026-72370-3 |
| 2026 | Adaptations in Plasmodium tubulin determine distinct microtubule architectures, mechanics and drug susceptibility. Nat Commun doi:10.1038/s41467-026-70181-0 |
| 2026 | Structure-based design and synthesis of 3-substituted-1,2,4-triazolo[1,5-a]pyrimidines as dual vinca/gatorbulin-site ligands for cancer treatment. Eur.J.Med.Chem. doi:10.1016/j.ejmech.2025.118245 |
| 2026 | Pathogenic KIF1A R350 mutations disrupt a conserved and conformation-dependent kinesin-tubulin salt bridge. Nat Commun doi:10.1038/s41467-026-71026-6 |
| 2026 | Atomic models of the Toxoplasma cell invasion machinery. Nat.Struct.Mol.Biol. doi:10.1038/s41594-025-01728-w |
| 2026 | SPACA9 and MNMIP1 bridge the seam of spermatid manchette microtubules. Embo J. doi:10.1038/s44318-026-00833-w |
| 2026 | Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility. Sci Rep doi:10.1038/s41598-025-28573-7 |
| 2026 | Hierarchical assembly of native cytoplasmic lattices revealed by cryo-EM Vita doi:10.15302/vita.2026.04.0030 |
| 2026 | Structural basis of microtubule-mediated signal transduction. Cell doi:10.1016/j.cell.2025.11.011 |
| 2026 | Cytoplasmic lattices store developmentally poised degradative and cytoskeletal complexes in mammalian eggs. Nat.Struct.Mol.Biol. doi:10.1038/s41594-026-01843-2 |
| 2026 | Structural basis of human gamma TuRC closure during CM1-activated microtubule nucleation. Nat Commun doi:10.1038/s41467-026-70773-w |
| 2026 | Doublet microtubule-associated tektins and enzymes differentially regulate sperm flagellar integrity and motility. Nat Commun doi:10.1038/s41467-026-69714-4 |
| 2026 | Structure of the mouse cytoplasmic lattice. Nature doi:10.1038/s41586-026-10442-6 |
| 2026 | Cytoplasmic lattices are megadalton storage complexes in mammalian oocytes. Nature doi:10.1038/s41586-026-10513-8 |
| 2026 | Molecular basis of oocyte cytoplasmic lattice assembly. Nature doi:10.1038/s41586-026-10360-7 |
| 2026 | In-situ cryo-ET of mouse embryos reveals cytoplasmic lattices contain ubiquitin-charged E2-E3 ligase assemblies. Embo J. doi:10.1038/s44318-026-00895-w |
| 2026 | In situ structure of the human ciliary transition zone links linker defects to primary ciliary dyskinesia. Science doi:10.1126/science.aei5957 |
| 2025 | Structure of quercetin 3,4'-dimethyl ether in complex with tubulin provides a rationale for drug design. Biochem.Biophys.Res.Commun. doi:10.1016/j.bbrc.2025.152245 |
| 2025 | Structural dissection of alpha beta-tubulin heterodimer assembly and disassembly by human tubulin-specific chaperones. Science doi:10.1126/science.ady2708 |
| 2025 | Effective Tubulin Degradation by Rationally Designed Proteolysis Targeting Chimeras Biorxiv doi:10.1101/2025.05.22.655572 |
| 2025 | Design and synthesis of novel 4-aryl-2-benzoyl-imidazoles as colchicine binding site inhibitors. Eur.J.Med.Chem. doi:10.1016/j.ejmech.2025.118021 |
| 2025 | Discovery of Kinesin KIF18A Inhibitor ATX020: Tactical Application of Silicon Atom Replacement. Acs Med.Chem.Lett. doi:10.1021/acsmedchemlett.5c00512 |
| 2025 | KY216-tubulin complex captures VASH2 to inhibit NSCLC metastasis. Nat Commun doi:10.1038/s41467-025-66817-2 |
| 2025 | Identification of a ligand-binding site on tubulin mediating the tubulin-RB3 interaction. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2424098122 |
| 2025 | Trypanosome doublet microtubule structures reveal flagellum assembly and motility mechanisms. Science doi:10.1126/science.adr3314 |
| 2025 | Evolutionary adaptations of doublet microtubules in trypanosomatid parasites. Science doi:10.1126/science.adr5507 |
| 2025 | Microtubule association induces a Mg-free apo-like ADP pre-release conformation in kinesin-1 that is unaffected by its autoinhibitory tail. Nat Commun doi:10.1038/s41467-025-61498-3 |
| 2025 | Mechanistic basis of temperature adaptation in microtubule dynamics across frog species. Curr.Biol. doi:10.1016/j.cub.2024.12.022 |
| 2025 | How augmin establishes the angle of the microtubule branch site. Nat Commun doi:10.1038/s41467-025-64650-1 |
| 2025 | Tubulin acetyltransferases access and modify the microtubule luminal K40 residue through anchors in taxane-binding pockets. Nat.Struct.Mol.Biol. doi:10.1038/s41594-024-01406-3 |
| 2025 | In situ structural mechanism of epothilone-B-induced CNS axon regeneration. Nature doi:10.1038/s41586-025-09654-z |
| 2025 | Dimerization of GAS2 mediates crosslinking of microtubules and F-actin. Embo J. doi:10.1038/s44318-025-00415-2 |
| 2025 | Mechanistic insights into TTLL11 polyglutamylase-mediated primary tubulin chain elongation. Sci Adv doi:10.1126/sciadv.adw1561 |